%0 Journal Article
%T Soluble Expression of Recombinant Human BMP6 in Escherichia coli and Its Purification and Bioassay in Vitro<br>重组人BMP6在大肠杆菌中可溶表达、纯化及活性分析
%A Rongyue Lei
%A Yuhuan Qiao
%A Jidong Yan
%A Shuang Yang
%A Tianhui Zhu
%A <br>雷荣悦
%A 乔玉欢
%A 闫继东
%A 杨爽
%A 朱天慧
%J 生物工程学报
%D 2008
%I 
%X BMP6 is a potent protein for future treatment strategies of bone regeneration as it is a very important regulator of bone homeostasis. Active BMP6 is a dimer containing multidisulfide bonds and is a highly hydrophobic protein prone to aggregation. To obtain soluble and active BMP6 in Escherichia coli, we compared the effects of four N-terminal fusion tags (TRX, GST, MBP and CBD) and N-terminal His6-tag. The expression and solubility were tested under the different conditions (expression hosts, temperatures and inductor concentrations). A series of experiments leads to the finding that the placement of MBP before the BMP6 is best in availing the soluble expression of the protein. Our study alsodemonstrates that in E. coli BL21trxB(DE3) cytoplasm, which is a thioredoxin reductase mutant strain, soluble homodimeric BMP6 can be formed. The overexpressed MBP-BMP6 fusion protein is purified by chromatography, and shown to be functionally active.
%K BMP6
%K MBP
%K BL21 trxB(DE3)
%K solubility<br>BMP6
%K MBP
%K BL21
%K trxB(DE3)
%K 可溶性
%K 重组人
%K 大肠杆菌
%K 可溶表达
%K 纯化
%K 活性分析
%K in
%K Vitro
%K Bioassay
%K Purification
%K Escherichia
%K coli
%K Human
%K Recombinant
%K 转化
%K 方向
%K 细胞系
%K 亲和层析
%K 凝胶排阻
%K 融合蛋白
%K 细胞质
%K 结合
%K 还原环境
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A66E90C274451689E69F6F0291467824&aid=EE1625B0E790B16B97865013251A8583&yid=67289AFF6305E306&vid=B91E8C6D6FE990DB&iid=38B194292C032A66&sid=30F3EEEA29E34EE7&eid=3389C664025A98F9&journal_id=1000-3061&journal_name=生物工程学报&referenced_num=0&reference_num=12